ID   A0A0N5B3P9_STREA        Unreviewed;       301 AA.
AC   A0A0N5B3P9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=PAP2_C domain-containing protein {ECO:0000313|WBParaSite:SPAL_0000070200.1};
OS   Strongyloides papillosus (Intestinal threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0000070200.1};
RN   [1] {ECO:0000313|WBParaSite:SPAL_0000070200.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC       {ECO:0000256|ARBA:ARBA00005441}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A0N5B3P9; -.
DR   STRING; 174720.A0A0N5B3P9; -.
DR   WBParaSite; SPAL_0000070200.1; SPAL_0000070200.1; SPAL_0000070200.
DR   Proteomes; UP000046392; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR045221; Sphingomyelin_synth-like.
DR   InterPro; IPR025749; Sphingomyelin_synth-like_dom.
DR   PANTHER; PTHR21290:SF4; SPHINGOMYELIN SYNTHASE-RELATED 2; 1.
DR   PANTHER; PTHR21290; SPHINGOMYELIN SYNTHETASE; 1.
DR   Pfam; PF14360; PAP2_C; 1.
PE   3: Inferred from homology;
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        101..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        191..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        216..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          162..233
FT                   /note="Sphingomyelin synthase-like"
FT                   /evidence="ECO:0000259|Pfam:PF14360"
SQ   SEQUENCE   301 AA;  34539 MW;  653F84561AD0C17E CRC64;
     MGNDTEALPG GGNLKSLDRS RTFVALLCLI FGWIFNIIVL AWVHDRVPRN DGPLPDLFFS
     LFPEVPNSIR ITEFIMLFMV INAVGIIYFH QHRWIVARRV FFCVAASYIF RAICICLLQV
     PVPSINTYCA PQQVSSFSVV SERVISTFWS AGIEALRPRV LCGDLIVSGH TICLFTALHT
     FKYYAPQKLR VLNTLYNIMA IIAIISILFA RKHYSIDVFL GYVVSTTIFR IYHSLMYSYH
     QNEMDKNLLS QNIISIFIPY FEKDALPPYL FVNMFHIPSL IKDRGPTKLC GYKKEFNNLN
     I
//